| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | NAD-dependent protein deacetylase sirtuin-1,hSIRT1,NAD-dependent protein deacylase sirtuin-1,Regulatory protein SIR2 homolog 1,SIR2-like protein 1|hSIR2),SIRT1,SIR2L1 |
| Assay Time | |
| Detection Method | |
| Detection Range | |
| Product Type | |
| Reactivity | |
| Sample Type(s) | Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples |
| Sensitivity | |
| Species | |
| Storage | |
| Target | |
| UniProt # |
Background
mouse Sirt1 (NAD-dependent deacetylase sirtuin-1) is a molecular target commonly studied in biomedical research. Many proteins are studied as molecular readouts that can change with cellular state, tissue remodeling, or stress responses.
Biological role and mechanism
The biological role of Sirt1 is typically understood in terms of its molecular category and interaction network. Depending on the model system, it may participate in cell–cell communication, intracellular signaling, enzymatic processing, or regulation of gene expression programs. Mechanistic interpretation is often strengthened by considering upstream regulators and downstream readouts rather than relying on a single marker.
Expression and abundance of Sirt1 can vary by tissue, cell type, and physiological state. In many systems, levels are influenced by factors such as developmental stage, immune activation, metabolic status, and cellular stress. Because sample matrix and pre-analytical handling can affect measured concentrations, interpretation is typically strongest when experiments keep collection and processing consistent across groups.
Nomenclature and related terms
Sirt1 (NAD-dependent deacetylase sirtuin-1) may also be referenced as NAD-dependent protein deacetylase sirtuin-1,hSIRT1,NAD-dependent protein deacylase sirtuin-1,Regulatory protein SIR2 homolog 1,SIR2-like protein 1 and hSIR2),SIRT1,SIR2L1 in the literature or in databases. When comparing results across studies, confirm that the reported analyte refers to the same molecule, species context, and molecular form (e.g., precursor vs mature protein, or soluble vs membrane-associated forms).
Why it matters in research
- Understanding how Sirt1 relates to signal transduction, tissue homeostasis, stress responses, and disease-model biology in biomedical research.
- Interpreting shifts in Sirt1 levels alongside other pathway components or complementary markers.
- Connecting molecular changes to phenotypes such as inflammation, remodeling, metabolism shifts, or cell-state transitions (context-dependent).
Molecular forms and interpretation
For some targets, isoforms, proteolytic processing, or post-translational modifications (such as phosphorylation or glycosylation) can influence function and apparent abundance. If multiple molecular forms are expected in your model, align interpretation with the form most relevant to the biological question.
Disease and translational relevance
Sirt1 has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with biomedical studies. These associations are interpreted as research findings rather than diagnostic or therapeutic claims, and they should be evaluated alongside model-specific covariates and study design.
Can’t Find What You’re Looking For? We can help you source the best match or customize an ELISA solution for your study. Options may include alternative target synonyms, different species reactivity, sample type/matrix compatibility (serum/plasma/lysate/supernatant), assay format (sandwich/competitive), sensitivity/range, detection chemistry (colorimetric/fluorescent/chemiluminescent), plate format (pre-coated/uncoated, strips vs full plate), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
Ginsenoside Rg1 Downregulates miR-9-5p Expression to Modulate SIRT1-Mediated Mitochondrial Dysfunction and Ameliorate Alzheimer's Disease
IF: 4.6 Journal: Molecular Neurobiology Author: College of Physical Education, AnHui Normal University, Wuhu, 241003, P.R. China. Cited Date: 2025-06-13
Involvement of the aryl hydrocarbon receptor (AhR) in the mechanism of action of elastin-derived peptide (VGVAPG) and its impact on neurosteroidogenesis
IF: 4.2 Journal: Neurochemistry International Author: Department of Biotechnology and Cell Biology, Medical College, University of Information Technology and Management in Rzeszow, Sucharskiego 2, 35-225, Rzeszow, Poland Cited Date: 2023-10-08
Involvement of sirtuins (Sirt1 and Sirt3) and aryl hydrocarbon receptor (AhR) in the effects of triclosan (TCS) on production of neurosteroids in primary mouse cortical neurons cultures
IF: 3.963 Journal: Pesticide Biochemistry and Physiology Cited Date: 2022-06-02